SitesBLAST
Comparing WP_010931960.1 NCBI__GCF_000006985.1:WP_010931960.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
51% identity, 96% coverage: 8:468/481 of query aligns to 9:462/478 of 3h0mA
- active site: K72 (= K76), S147 (= S151), S148 (= S152), S166 (= S170), T168 (= T172), G169 (= G173), G170 (= G174), S171 (= S175), Q174 (= Q178)
- binding glutamine: M122 (= M126), G123 (= G127), D167 (= D171), T168 (= T172), G169 (= G173), G170 (= G174), S171 (= S175), F199 (= F203), Y302 (= Y307), R351 (= R356), D418 (= D423)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
51% identity, 96% coverage: 8:468/481 of query aligns to 9:462/478 of 3h0lA
- active site: K72 (= K76), S147 (= S151), S148 (= S152), S166 (= S170), T168 (= T172), G169 (= G173), G170 (= G174), S171 (= S175), Q174 (= Q178)
- binding asparagine: G123 (= G127), S147 (= S151), G169 (= G173), G170 (= G174), S171 (= S175), Y302 (= Y307), R351 (= R356), D418 (= D423)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
44% identity, 98% coverage: 1:473/481 of query aligns to 3:474/485 of 2f2aA
- active site: K79 (= K76), S154 (= S151), S155 (= S152), S173 (= S170), T175 (= T172), G176 (= G173), G177 (= G174), S178 (= S175), Q181 (= Q178)
- binding glutamine: G130 (= G127), S154 (= S151), D174 (= D171), T175 (= T172), G176 (= G173), S178 (= S175), F206 (= F203), Y309 (= Y307), Y310 (= Y308), R358 (= R356), D425 (= D423)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
44% identity, 98% coverage: 1:473/481 of query aligns to 3:474/485 of 2dqnA
- active site: K79 (= K76), S154 (= S151), S155 (= S152), S173 (= S170), T175 (= T172), G176 (= G173), G177 (= G174), S178 (= S175), Q181 (= Q178)
- binding asparagine: M129 (= M126), G130 (= G127), T175 (= T172), G176 (= G173), S178 (= S175), Y309 (= Y307), Y310 (= Y308), R358 (= R356), D425 (= D423)
3kfuE Crystal structure of the transamidosome (see paper)
45% identity, 95% coverage: 8:465/481 of query aligns to 4:447/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
35% identity, 83% coverage: 68:465/481 of query aligns to 30:443/450 of 4n0iA
- active site: K38 (= K76), S116 (= S151), S117 (= S152), T135 (≠ S170), T137 (= T172), G138 (= G173), G139 (= G174), S140 (= S175), L143 (≠ Q178)
- binding glutamine: G89 (= G127), T137 (= T172), G138 (= G173), S140 (= S175), Y168 (≠ F203), Y271 (= Y307), Y272 (= Y308), R320 (= R356), D404 (= D423)
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
30% identity, 97% coverage: 10:474/481 of query aligns to 139:590/607 of Q7XJJ7
- K205 (= K76) mutation to A: Loss of activity.
- SS 281:282 (= SS 151:152) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 172:175) binding substrate
- S305 (= S175) mutation to A: Loss of activity.
- R307 (= R177) mutation to A: Loss of activity.
- S360 (≠ K230) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
30% identity, 97% coverage: 10:474/481 of query aligns to 139:590/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A125), T258 (≠ S128), S281 (= S151), G302 (≠ T172), G303 (= G173), S305 (= S175), S472 (≠ T361), I532 (≠ P416), M539 (≠ D423)
Sites not aligning to the query:
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
29% identity, 97% coverage: 10:474/481 of query aligns to 139:590/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A125), G302 (≠ T172), G303 (= G173), G304 (= G174), A305 (≠ S175), V442 (≠ Y308), I475 (≠ L364), M539 (≠ D423)
Sites not aligning to the query:
8ey1D Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with n-(3-oxododecanoyl)-l-homoserine lactone
29% identity, 97% coverage: 10:474/481 of query aligns to 139:590/605 of 8ey1D
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
31% identity, 86% coverage: 66:480/481 of query aligns to 85:505/508 of 3a1iA
- active site: K95 (= K76), S170 (= S151), S171 (= S152), G189 (≠ S170), Q191 (≠ T172), G192 (= G173), G193 (= G174), A194 (≠ S175), I197 (≠ Q178)
- binding benzamide: F145 (≠ M126), S146 (≠ G127), G147 (≠ S128), Q191 (≠ T172), G192 (= G173), G193 (= G174), A194 (≠ S175), W327 (≠ Y307)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
30% identity, 95% coverage: 15:472/481 of query aligns to 12:448/457 of 6c6gA
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
31% identity, 96% coverage: 8:468/481 of query aligns to 10:472/487 of 1m21A
- active site: K81 (= K76), S160 (= S151), S161 (= S152), T179 (≠ S170), T181 (= T172), D182 (≠ G173), G183 (= G174), S184 (= S175), C187 (≠ Q178)
- binding : A129 (= A125), N130 (≠ M126), F131 (≠ G127), C158 (≠ G149), G159 (= G150), S160 (= S151), S184 (= S175), C187 (≠ Q178), I212 (≠ F203), R318 (≠ Y308), L321 (≠ V311), L365 (≠ M358), F426 (≠ N415)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
32% identity, 94% coverage: 19:472/481 of query aligns to 17:438/461 of 4gysB
- active site: K72 (= K76), S146 (= S151), S147 (= S152), T165 (≠ S170), T167 (= T172), A168 (≠ G173), G169 (= G174), S170 (= S175), V173 (≠ Q178)
- binding malonate ion: A120 (= A125), G122 (= G127), S146 (= S151), T167 (= T172), A168 (≠ G173), S170 (= S175), S193 (≠ Y198), G194 (= G199), V195 (≠ L200), R200 (≠ S205), Y297 (= Y307), R305 (≠ T312)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
29% identity, 96% coverage: 18:480/481 of query aligns to 42:495/507 of Q84DC4
- K100 (= K76) mutation to A: Abolishes activity on mandelamide.
- S180 (= S151) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S152) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G173) mutation to A: Increase in KM values for aromatic substrates, but not aliphatic substrates. Active against lactamide but not against mandelamide; when associated with H-207 and E-382.; mutation to V: Increase in KM values for aromatic substrates, but not aliphatic substrates.
- S204 (= S175) mutation to A: Abolishes activity on mandelamide.
- Q207 (= Q178) mutation to H: Increases activity on lactamide, does not affect activity on mandelamide; when associated with E-382. Active against lactamide but not against mandelamide; when associated with A-202 and E-382. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with S-316 and N-437.
- S316 (≠ A303) mutation to N: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with H-207 and N-437.
- Q382 (≠ G367) mutation to H: Increases activity on lactamide, does not affect activity on mandelamide; when associated with H-207. Active against lactamide but not against mandelamide; when associated with A-202 and H-207.
- I437 (≠ V427) mutation to N: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with I-31. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with H-207 and N-316.
Sites not aligning to the query:
- 31 T→I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
31% identity, 93% coverage: 23:469/481 of query aligns to 38:458/605 of Q936X2
- K91 (= K76) mutation to A: Loss of activity.
- S165 (= S151) mutation to A: Loss of activity.
- S189 (= S175) mutation to A: Loss of activity.
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
25% identity, 91% coverage: 8:447/481 of query aligns to 9:428/457 of 5h6sC
- active site: K77 (= K76), S152 (= S151), S153 (= S152), L173 (≠ T172), G174 (= G173), G175 (= G174), S176 (= S175)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A125), R128 (≠ G127), W129 (≠ S128), S152 (= S151), L173 (≠ T172), G174 (= G173), S176 (= S175), W306 (≠ Y307), F338 (≠ L359)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
27% identity, 97% coverage: 8:472/481 of query aligns to 6:407/412 of 1o9oA
- active site: K62 (= K76), A131 (≠ S151), S132 (= S152), T150 (≠ S170), T152 (= T172), G153 (= G173), G154 (= G174), S155 (= S175), R158 (≠ Q178)
- binding 3-amino-3-oxopropanoic acid: G130 (= G150), T152 (= T172), G153 (= G173), G154 (= G174), S155 (= S175), R158 (≠ Q178), P359 (≠ K412)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
27% identity, 97% coverage: 8:472/481 of query aligns to 6:407/412 of 1ocmA
- active site: K62 (= K76), S131 (= S151), S132 (= S152), T152 (= T172), G153 (= G173), G154 (= G174), S155 (= S175)
- binding pyrophosphate 2-: R113 (≠ S129), S131 (= S151), Q151 (≠ D171), T152 (= T172), G153 (= G173), G154 (= G174), S155 (= S175), R158 (≠ Q178), P359 (≠ K412)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
26% identity, 92% coverage: 15:455/481 of query aligns to 17:456/490 of 4yjiA
- active site: K79 (= K76), S158 (= S151), S159 (= S152), G179 (≠ T172), G180 (= G173), G181 (= G174), A182 (≠ S175)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ N78), G132 (≠ A125), S158 (= S151), G179 (≠ T172), G180 (= G173), A182 (≠ S175)
Query Sequence
>WP_010931960.1 NCBI__GCF_000006985.1:WP_010931960.1
MQFHGYEDLRSRLLSGELTCEQVISDYLQRIDSSRDDNIFTVVFHDEAMARARELDSKLQ
RGEAPGVLFGMPIAIKDNIAMKGAPLSCASKILAGYESVYDATVIKRMQAEDAIFVGRTN
MDEFAMGSSNENSAIGPVPNPYDKTRVPGGSSGGSAAAVANDLAMVALGSDTGGSVRQPA
GFCNIIGLKPTYGRISRYGLVAFASSFDQIGLLAANCDDAALVLGVIAGKDEHDATSSHH
DVPEYDTAMDHVSVDGLRIGVPRAFFPESLNADVAGVVKAGLKKLEEAGAELVEIDLPES
DYAIAAYYILVTAEASSNLARFDGARYGYRSPDSPDLSSMYVNSRTEGFGAEVKRRIMLG
TYVLSAGYYDTYYKKAQQVRRVFQDKYREAFEKVDVIFGPTSPFPPFGIGDKMDNPLEMY
LADVFTVPASIVGMPAISVPVGFDSLGLPVGAHLICNFFEEGKMLGIARHLQTLCQTAPS
N
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory